Effect of Postmortem Storage on Cold‐Shortened Bovine Muscle: Analysis by SDS‐Polyacrylamide...
KOOHMARAIE, M.; KENNICK, W. H.; ANGLEMIER, A. F.; ELGASIM, E. A.; JONES, T. K.
1984-01-01 00:00:00
ABSTRACT Myofibrils were isolated from the longissimus (L) muscle of control (CON) and cold‐shortened (CS) muscles after 0, 1, 3, 7, and 10 days of postmortem storage at 2°C. Isolated myofibrils were then examined by SDS‐polyacrylamide gel electrophoresis to monitor the changes in the myofibrillar proteins during postmortem storage. The main changes in CS muscles were the gradual appearance of 110,000‐, 95,000‐, and 30,000d‐dalton components and the disappearance of desmin and troponin‐T components of myofibrils. In addition, there was a gradual increase in the intensity of a protein around 55,000‐daltons. CON samples showed similar changes to those of CS samples. It appears that myofibrillar proteins of cold‐shortened muscles are affected by postmortem aging in a manner similar to that of the normally chilled muscles.
http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.pngJournal of Food ScienceWileyhttp://www.deepdyve.com/lp/wiley/effect-of-postmortem-storage-on-cold-shortened-bovine-muscle-analysis-yz2VIOCcrS

Abstract

ABSTRACT Myofibrils were isolated from the longissimus (L) muscle of control (CON) and cold‐shortened (CS) muscles after 0, 1, 3, 7, and 10 days of postmortem storage at 2°C. Isolated myofibrils were then examined by SDS‐polyacrylamide gel electrophoresis to monitor the changes in the myofibrillar proteins during postmortem storage. The main changes in CS muscles were the gradual appearance of 110,000‐, 95,000‐, and 30,000d‐dalton components and the disappearance of desmin and troponin‐T components of myofibrils. In addition, there was a gradual increase in the intensity of a protein around 55,000‐daltons. CON samples showed similar changes to those of CS samples. It appears that myofibrillar proteins of cold‐shortened muscles are affected by postmortem aging in a manner similar to that of the normally chilled muscles.